New insight into the recognition of branched DNA structure by junction-resolving enzymes

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    61 Citations (Scopus)

    Abstract

    Junction-resolving enzymes are nucleases that exhibit structural selectivity for the four-way (Holliday) junction in DNA. In general, these enzymes both recognize and distort the structure of the junction. New insight into the molecular recognition processes has been provided by two recent co-crystal structures of resolving enzymes bound to four-way DNA junctions in highly contrasting ways. T4 endonuclease VII binds the junction in an open conformation to an approximately flat binding surface whereas T7 enclonuclease I envelops the junction, which retains a much more three-dimensional structure. Both proteins make contacts with the DNA backbone over an extensive area in order to generate structural specificity. The comparison highlights the versatility of Holliday junction resolution, and extracts some general principles of recognition.

    Original languageEnglish
    Pages (from-to)86-95
    Number of pages10
    JournalCurrent Opinion in Structural Biology
    Volume18
    Issue number1
    DOIs
    Publication statusPublished - Feb 2008

    Keywords

    • T4 ENDONUCLEASE VII
    • HOLLIDAY JUNCTION
    • CRYSTAL-STRUCTURE
    • T7 ENDONUCLEASE
    • ESCHERICHIA-COLI
    • SULFOLOBUS-SOLFATARICUS
    • SUBSTRATE-SPECIFICITY
    • NUCLEIC-ACIDS
    • ACTIVE-SITE
    • BINDING

    Cite this

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    title = "New insight into the recognition of branched DNA structure by junction-resolving enzymes",
    abstract = "Junction-resolving enzymes are nucleases that exhibit structural selectivity for the four-way (Holliday) junction in DNA. In general, these enzymes both recognize and distort the structure of the junction. New insight into the molecular recognition processes has been provided by two recent co-crystal structures of resolving enzymes bound to four-way DNA junctions in highly contrasting ways. T4 endonuclease VII binds the junction in an open conformation to an approximately flat binding surface whereas T7 enclonuclease I envelops the junction, which retains a much more three-dimensional structure. Both proteins make contacts with the DNA backbone over an extensive area in order to generate structural specificity. The comparison highlights the versatility of Holliday junction resolution, and extracts some general principles of recognition.",
    keywords = "T4 ENDONUCLEASE VII, HOLLIDAY JUNCTION, CRYSTAL-STRUCTURE, T7 ENDONUCLEASE, ESCHERICHIA-COLI, SULFOLOBUS-SOLFATARICUS, SUBSTRATE-SPECIFICITY, NUCLEIC-ACIDS, ACTIVE-SITE, BINDING",
    author = "Anne-Cecile Declais and Lilley, {David M. J.}",
    year = "2008",
    month = "2",
    doi = "10.1016/j.sbi.2007.11.001",
    language = "English",
    volume = "18",
    pages = "86--95",
    journal = "Current Opinion in Structural Biology",
    issn = "0959-440X",
    publisher = "Elsevier",
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    }

    TY - JOUR

    T1 - New insight into the recognition of branched DNA structure by junction-resolving enzymes

    AU - Declais, Anne-Cecile

    AU - Lilley, David M. J.

    PY - 2008/2

    Y1 - 2008/2

    N2 - Junction-resolving enzymes are nucleases that exhibit structural selectivity for the four-way (Holliday) junction in DNA. In general, these enzymes both recognize and distort the structure of the junction. New insight into the molecular recognition processes has been provided by two recent co-crystal structures of resolving enzymes bound to four-way DNA junctions in highly contrasting ways. T4 endonuclease VII binds the junction in an open conformation to an approximately flat binding surface whereas T7 enclonuclease I envelops the junction, which retains a much more three-dimensional structure. Both proteins make contacts with the DNA backbone over an extensive area in order to generate structural specificity. The comparison highlights the versatility of Holliday junction resolution, and extracts some general principles of recognition.

    AB - Junction-resolving enzymes are nucleases that exhibit structural selectivity for the four-way (Holliday) junction in DNA. In general, these enzymes both recognize and distort the structure of the junction. New insight into the molecular recognition processes has been provided by two recent co-crystal structures of resolving enzymes bound to four-way DNA junctions in highly contrasting ways. T4 endonuclease VII binds the junction in an open conformation to an approximately flat binding surface whereas T7 enclonuclease I envelops the junction, which retains a much more three-dimensional structure. Both proteins make contacts with the DNA backbone over an extensive area in order to generate structural specificity. The comparison highlights the versatility of Holliday junction resolution, and extracts some general principles of recognition.

    KW - T4 ENDONUCLEASE VII

    KW - HOLLIDAY JUNCTION

    KW - CRYSTAL-STRUCTURE

    KW - T7 ENDONUCLEASE

    KW - ESCHERICHIA-COLI

    KW - SULFOLOBUS-SOLFATARICUS

    KW - SUBSTRATE-SPECIFICITY

    KW - NUCLEIC-ACIDS

    KW - ACTIVE-SITE

    KW - BINDING

    U2 - 10.1016/j.sbi.2007.11.001

    DO - 10.1016/j.sbi.2007.11.001

    M3 - Review article

    VL - 18

    SP - 86

    EP - 95

    JO - Current Opinion in Structural Biology

    JF - Current Opinion in Structural Biology

    SN - 0959-440X

    IS - 1

    ER -